VWFC domain signature and profile

The VWFC domain is named after the von Willebrand factor (VWF) type C repeat
which is found twice in this multidomain protein [1,2]. It has a length of
about 70 amino acids covering 10 well conserved cysteines. Proteins with such
a domain [1,2,3,4] are listed below.

Silk moth hemocytin, an humoral lectin which is involved in a self-defence
mechanism. It is composed of 2 FA58C domains (see <PDOC00988>), a C-type
lectin domain (see <PDOC00537>), 2 VWFC domains, and a CTCK (see
<PDOC00912>).

Several vertebrate heavily glycosylated mucins. Human mucin 2 is secreted
by the epithelia of different mucus membrane-containing organs. It is a
highly polymorphic multidomain molecule. Rat intestinal mucin-like peptide
coats the epithelia of the intestines. Both proteins share a modular
architecture similar to VWF. Xenopus mucin B.1 contains a Sushi domain, a
VWFC domain, a X domain and a C-terminal cystine knot. Other mucins that
contain the VWFC domain are human tracheobronchial mucin (MUC5), bovine
submaxillary mucin-like protein, human and pig apomucin.

Cef-10/cyr61/CTGF/fisp-12/nov protein family. The members of this family
are structurally related to insulin-like growth factor binding proteins
(see <PDOC00194>) and could function as growth factor-binding proteins.
They contain an insulin-like growth factor-binding domain, a VWFC repeat, a
thrombospondin type 1 repeat (Tsp1) and a C-terminal cystine knot.

Chordin, a Xenopus developmental protein that contains four VWFC domains.

Of these proteins, the best characterized one is the von Willebrand factor for
which the duplicated VWFC domain is thought to participate in oligomerization,
but not in the initial dimerization step [4]. The presence of this region in
other complex-forming proteins leads to the assumption that the VWFC domain
might be involved in forming larger protein complexes [1,2].

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